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Database: UniProt
Entry: A0A1I8IHS7_9PLAT
LinkDB: A0A1I8IHS7_9PLAT
Original site: A0A1I8IHS7_9PLAT 
ID   A0A1I8IHS7_9PLAT        Unreviewed;      1519 AA.
AC   A0A1I8IHS7;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=LamGL domain-containing protein {ECO:0000313|WBParaSite:maker-uti_cns_0012677-snap-gene-0.2-mRNA-1};
OS   Macrostomum lignano.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC   Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX   NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0012677-snap-gene-0.2-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:maker-uti_cns_0012677-snap-gene-0.2-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00152}.
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DR   WBParaSite; maker-uti_cns_0012677-snap-gene-0.2-mRNA-1; maker-uti_cns_0012677-snap-gene-0.2-mRNA-1; maker-uti_cns_0012677-snap-gene-0.2.
DR   Proteomes; UP000095280; Unplaced.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd01756; PLAT_repeat; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.40.180.10; Catalase core domain; 2.
DR   Gene3D; 2.60.60.20; PLAT/LH2 domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR006558; LamG-like.
DR   InterPro; IPR001024; PLAT/LH2_dom.
DR   InterPro; IPR036392; PLAT/LH2_dom_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR45901:SF6; LIPOXYGENASE HOMOLOGY DOMAIN-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR45901; PROTEIN CBG12474; 1.
DR   Pfam; PF13385; Laminin_G_3; 1.
DR   Pfam; PF01477; PLAT; 2.
DR   SMART; SM00560; LamGL; 1.
DR   SMART; SM00308; LH2; 2.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR   SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 3.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50095; PLAT; 2.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          1072..1123
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          1207..1337
FT                   /note="PLAT"
FT                   /evidence="ECO:0000259|PROSITE:PS50095"
FT   DOMAIN          1403..1519
FT                   /note="PLAT"
FT                   /evidence="ECO:0000259|PROSITE:PS50095"
FT   REGION          975..1003
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1021..1042
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1239..1278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1021..1035
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1519 AA;  164980 MW;  948D353C75111FD5 CRC64;
     MTEPLQRLVA AQLLTNSNIN GHRDAKWNLT RTEYITIRPR CRYMPMRFLL RLPNVWENRV
     SQAVLMPTPM QMPATANMTK NSSRNPNGNI RSQSLLAIAT SRLLLSVSST TPSSVQFAHE
     VKAVAEPLVA EPLVACRVPL TRILTSGVCL SYTAAIWVQP LAVSVGPDTE TFDTTVEMAA
     VRDRIASPSG VAHGPEGDEA ELAQGAPRLA VGAVRQTGRL EAVRHVADAC AVAPGDAGTT
     ELRAQEGAHA GARGRQGVLR SLRHHAAAER DAAVQLAAGL GNGGQKEKKK QKRRAVAAHF
     LQKFSVTNGG CLMVEASQQL KASSACFCAS LCSSRSSCIG WSYRHGRCNV SDSVHTVWTN
     NASCKMWSRL RELGFVAFWP MSNATRTRNA VPNSGHLDLQ ENIPMQYTDS AVNFTGQSDV
     PERFNIDELT SVCLTSLTMS VWVKVTNASR GSMPLLEGLT MPSSYHTRFW LYPTATNIEF
     TVVSKVSVSG PTDTASGWTH IAAVYDKQTP EIRILVNGTR QATSGSAAAL TSCANFGSSV
     QIGAVSRNAG HNRVFEGFMR CFGVSERALR DSEVALLQGL ALADTLKQRI WPRNTRLCGV
     ERTMAPISTV EPKLTHEFTV EATEVVVLTG VPLMYSVVEM AAVRDRIASP SGVAHGPEGD
     EAELAQGAPR LAVGVVRQTG GLEAVRHVAD ACAVAPGDAG TTELRAQKGA HAGARGRQRV
     LRSLRHHAAA DRDVSVQLAA ELQANASMSW WELPKMEKSF SDSTFVSAQK FSVTNGGCLM
     VEASQQLKAS SACFCASLCS SRSSCIGWSY RHGRCNVSDS VHTVWTNNAS CKMWSRLREL
     GFVAFWPMSN ATRTRNAVPN SGHLDLQENI PLQYTDNAVN FTGQSDVSER FNIDELTSVC
     LTSFTMSVWV KVTNSTRGPM PLLEGLSMPD QYFTRLWLYP DTTNLQFVIG TAEFAKTVSG
     LTSTSLVLPA PADAAATASN QHQQHRWIPA PSLASPPPPQ QHPRQLYAQL QQLYRRRLRT
     VETDVNDDDD ADGSRPVSSD SGISDCCCIN QQQLQRSQQQ TPSDTDAAAP ACRICLTSLS
     KVGPSAAANC GHVACLPCLL AWYRTRDSTP LLKRPAMHPP HCPFSSKFPH ADQQLCSHRS
     SLEPASGRSR AALPTYSSLE DPHLVDYFER KFGNVTGSYA SRLGIGGFGA SGAVGSRGRS
     GRSGQEVTYK LSITTADSEG SGTDAPVFVS LHGSHGTMGR RKLAKKSASA GRKPRAAGGG
     GGFRFRRGST NSFKMKSPDL GDLQSLTVEN AGTEERDSWL LQSVEVTNLV SKKTWLFLNN
     RWLSLFKEDC KTVRQLGAIK CSKTSYEVLV FTGDQDGAGT DSRIFLTLFG QAGVTRRLPL
     RSDFQTVREL VASREPGAAP KNTTFKIKVY TGDKAGAGTD ADVFLKLTGD KADSNDIALN
     EPTMGGRNLF ERNSVDEFMY KSRYLGQLQR ARVWHNNKGF APGWYLEKLI VEDLAMGRVY
     EFPCAQWLAD SEGDRKTSR
//
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